Psychrophiles: A journey of hope

Tendulkar, Shivani; Hattiholi, Aishwarya; Chavadar, Mahesh S.; Dodamani, Suneel

doi:10.1007/s12038-021-00180-4

Cited by 9 publications

(5 citation statements)

References 73 publications

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“…Finally, new insights into cold transitions and the future development of theory to predict energy landscape and structural features of LELS states promise to (i) enhance our understanding of the role of cold transitions in biomedical research, for example, for amyloid fibril homeostasis or vaccine development, , (ii) provide new insights into the functioning of psychrophilic proteins, and (iii) support the engineering of cold-adapted enzymes and ice-binding proteins . The use of protein design has proven to be a significant, efficient, and effective means to enhance our understanding of protein cold transitions.…”

Section: Discussionmentioning

confidence: 99%

From Protein Design to the Energy Landscape of a Cold Unfolding Protein

et al. 2022

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Understanding protein folding is crucial for protein sciences. The conformational spaces and energy landscapes of cold (unfolded) protein states, as well as the associated transitions, are hardly explored. Furthermore, it is not known how structure relates to the cooperativity of cold transitions, if cold and heat unfolded states are thermodynamically similar, and if cold states play important roles for protein function. We created the cold unfolding 4-helix bundle DCUB1 with a de novo designed bipartite hydrophilic/hydrophobic core featuring a hydrogen bond network which extends across the bundle in order to study the relative importance of hydrophobic versus hydrophilic protein–water interactions for cold unfolding. Structural and thermodynamic characterization resulted in the discovery of a complex energy landscape for cold transitions, while the heat unfolded state is a random coil. Below ∼0 °C, the core of DCUB1 disintegrates in a largely cooperative manner, while a near-native helical content is retained. The resulting cold core-unfolded state is compact and features extensive internal dynamics. Below −5 °C, two additional cold transitions are seen, that is, (i) the formation of a water-mediated, compact, and highly dynamic dimer, and (ii) the onset of cold helix unfolding decoupled from cold core unfolding. Our results suggest that cold unfolding is initiated by the intrusion of water into the hydrophilic core network and that cooperativity can be tuned by varying the number of core hydrogen bond networks. Protein design has proven to be invaluable to explore the energy landscapes of cold states and to robustly test related theories.

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Section: Discussionmentioning

confidence: 99%

From Protein Design to the Energy Landscape of a Cold Unfolding Protein

et al. 2022

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“…Since most antibacterial agents come from well-known terrestrial or aquatic actinomycete isolates [20], researchers focused on microorganisms isolated from unusual habitats [21]. The search for new bioactive molecules has shifted toward marine ecosystems [22][23][24], taxa living in extreme environments [25][26][27][28], plant-associated endophytes [29,30] and epiphytes [31], and hard-to-reach habitats (such as karst caves) [32]. Another step at which some potentially valuable antibiotic metabolites are lost is primary screening.…”

Section: Exploring New Habitatsmentioning

confidence: 99%

Modern Trends in Natural Antibiotic Discovery

Baranova

Alferova

Korshun

et al. 2023

Life

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Natural scaffolds remain an important basis for drug development. Therefore, approaches to natural bioactive compound discovery attract significant attention. In this account, we summarize modern and emerging trends in the screening and identification of natural antibiotics. The methods are divided into three large groups: approaches based on microbiology, chemistry, and molecular biology. The scientific potential of the methods is illustrated with the most prominent and recent results.

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“…56,57 Enzymes from psychrophiles can operate at much lower temperature, obviating the need for sanitisation between production cycles in food/milk processing industries. [58][59][60][61][62][63][64] Enzymes from psychrophiles are also useful in washing machine detergents. According to Novozyme, "if everybody in Europe turned down the wash temperature from 60 to 40 °C and from 40 to 30 °C, the carbon dioxide reduction would equal the annual carbon emissions from 3 million cars" (Biotimes, no.…”

Section: Economics Of Biocatalytic Processesmentioning

confidence: 99%